ID W0RVP4_9BACT Unreviewed; 575 AA.
AC W0RVP4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=J421_6118 {ECO:0000313|EMBL:AHG93653.1};
OS Gemmatirosa kalamazoonensis.
OG Plasmid 2 {ECO:0000313|EMBL:AHG93653.1, ECO:0000313|Proteomes:UP000019151}.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatirosa.
OX NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG93653.1, ECO:0000313|Proteomes:UP000019151};
RN [1] {ECO:0000313|EMBL:AHG93653.1, ECO:0000313|Proteomes:UP000019151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS708 {ECO:0000313|EMBL:AHG93653.1,
RC ECO:0000313|Proteomes:UP000019151};
RC PLASMID=Plasmid 2 {ECO:0000313|Proteomes:UP000019151};
RX PubMed=24699952;
RA Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA Fawaz M.N., Korlach J., Tsai Y.C.;
RT "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT Phylum.";
RL Genome Announc. 2:e00226-14(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|RuleBase:RU361134};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; CP007130; AHG93653.1; -; Genomic_DNA.
DR AlphaFoldDB; W0RVP4; -.
DR KEGG; gba:J421_6118; -.
DR PATRIC; fig|861299.3.peg.6176; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_2_1_0; -.
DR InParanoid; W0RVP4; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000019151; Plasmid 2.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11334; AmyAc_TreS; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|RuleBase:RU361134};
KW Plasmid {ECO:0000313|EMBL:AHG93653.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019151}.
FT DOMAIN 16..417
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 575 AA; 63797 MW; 56553D23C1C9F5C4 CRC64;
MLGPGDLWYK SAAIYAINVD TFRDADGDGV GDFSGLTSRV DYLHALGVTC VWLLPFYPSP
NRDNRYDVAD YYGVDPRLGT LGDFVDFLRV ARERGIRVMI DLVVNHTSDQ HPWFQAARAD
RASRYRDYYV WADEPPPNAR EGMVFPGVEE STWSYDDVAG AWYFHRFYRF QPDLNLANPA
VREEIRKIMG FWLELGVSGF RLDAAPFLIE RKGVSAAVVE ARRPHTFFRY MRSFLSWRRG
DAALLAEANV LPDEVEDYVG SGDKLQLLFN FYANQHLFLS LATGRAAPLV EALGALPALP
PSAQWANFLR NHDELDLGRL TDDDRGACYD AFAPDVDMRL YGRGVRRRLA PMLGNDRARL
ELAHSLMLAL PGTPVLRYGD EIGMGDDLSL PEREGVRTPM QWTRGPNGGF STAPPERLVR
PMVTGEYGPD AVNVADQQRD PGSLLNWLQR ALGVRHGCPE IGWGSGRAIA VDVPSVVAIR
CDWRTRHAAV VPTPVGEIGA PDGPSAVITL HNLAPEPCTV CLAASDVGPG EVTELLTDRD
YGRAPDLRGE VALGPYGYRW FRIATGDDRS TGPGR
//